ID   LAM1_COCH4              Reviewed;         475 AA.
AC   N4WEA4; C3PTB1;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2013, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=3-hydroxyacyl-CoA dehydrogenase-like protein LAM1 {ECO:0000303|PubMed:16529376};
DE            EC=1.1.-.- {ECO:0000305|PubMed:16529376};
DE   AltName: Full=T-toxin biosynthesis protein LAM1 {ECO:0000305};
GN   Name=LAM1 {ECO:0000303|PubMed:16529376}; ORFNames=COCC4DRAFT_67231;
OS   Cochliobolus heterostrophus (strain C4 / ATCC 48331 / race T) (Southern
OS   corn leaf blight fungus) (Bipolaris maydis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=665024;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=C4 / ATCC 48331 / race T;
RX   PubMed=20192833; DOI=10.1094/mpmi-23-4-0458;
RA   Inderbitzin P., Asvarak T., Turgeon B.G.;
RT   "Six new genes required for production of T-toxin, a polyketide determinant
RT   of high virulence of Cochliobolus heterostrophus to maize.";
RL   Mol. Plant Microbe Interact. 23:458-472(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C4 / ATCC 48331 / race T;
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C4 / ATCC 48331 / race T;
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
RN   [4]
RP   FUNCTION.
RC   STRAIN=C4 / ATCC 48331 / race T;
RX   PubMed=8953776; DOI=10.2307/3870419;
RA   Yang G., Rose M.S., Turgeon B.G., Yoder O.C.;
RT   "A polyketide synthase is required for fungal virulence and production of
RT   the polyketide T-toxin.";
RL   Plant Cell 8:2139-2150(1996).
RN   [5]
RP   FUNCTION.
RC   STRAIN=C4 / ATCC 48331 / race T;
RX   PubMed=12236595; DOI=10.1094/mpmi.2002.15.9.883;
RA   Rose M.S., Yun S.-H., Asvarak T., Lu S.-W., Yoder O.C., Turgeon B.G.;
RT   "A decarboxylase encoded at the Cochliobolus heterostrophus translocation-
RT   associated Tox1B locus is required for polyketide (T-toxin) biosynthesis
RT   and high virulence on T-cytoplasm maize.";
RL   Mol. Plant Microbe Interact. 15:883-893(2002).
RN   [6]
RP   FUNCTION.
RX   PubMed=16529376; DOI=10.1094/mpmi-19-0139;
RA   Baker S.E., Kroken S., Inderbitzin P., Asvarak T., Li B.Y., Shi L.,
RA   Yoder O.C., Turgeon B.G.;
RT   "Two polyketide synthase-encoding genes are required for biosynthesis of
RT   the polyketide virulence factor, T-toxin, by Cochliobolus heterostrophus.";
RL   Mol. Plant Microbe Interact. 19:139-149(2006).
CC   -!- FUNCTION: 3-hydroxyacyl-CoA dehydrogenase-like protein; part of the
CC       Tox1A locus, one of the 2 loci that mediate the biosynthesis of T-
CC       toxin, a family of linear polyketides 37 to 45 carbons in length, of
CC       which the major component is 41 carbons, and which leads to high
CC       virulence to maize (PubMed:8953776, PubMed:20192833). One of the PKSs
CC       (PKS1 or PKS2) could synthesize a precursor, used subsequently by the
CC       other PKS as starter unit, to add additional carbons (PubMed:16529376).
CC       Variability in the length of the final carbon backbone C35-47 could be
CC       achieved by varying the number of condensation cycles, or use of
CC       different starter or extender units or might be due to decarboxylation
CC       of the penultimate product, catalyzed by DEC1 (PubMed:12236595).
CC       Additional proteins are required for the biosynthesis of T-toxin,
CC       including oxidoreductases RED1, RED2, RED3, LAM1 and OXI1, as well as
CC       esterase TOX9 (PubMed:20192833). {ECO:0000269|PubMed:12236595,
CC       ECO:0000269|PubMed:16529376, ECO:0000269|PubMed:20192833,
CC       ECO:0000269|PubMed:8953776}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:20192833}.
CC   -!- DISRUPTION PHENOTYPE: Significantly reduces the production of T-toxin
CC       and decreases the virulence to maize (PubMed:20192833).
CC       {ECO:0000269|PubMed:20192833}.
CC   -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; DQ186598; ACP43390.1; -; Genomic_DNA.
DR   EMBL; KB733526; ENH98578.1; -; Genomic_DNA.
DR   RefSeq; XP_014072488.1; XM_014217013.1.
DR   AlphaFoldDB; N4WEA4; -.
DR   SMR; N4WEA4; -.
DR   EnsemblFungi; ENH98578; ENH98578; COCC4DRAFT_67231.
DR   GeneID; 25847228; -.
DR   HOGENOM; CLU_031652_0_0_1; -.
DR   OrthoDB; 314267at2759; -.
DR   PHI-base; PHI:2834; -.
DR   Proteomes; UP000012338; Unassembled WGS sequence.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   Gene3D; 2.120.10.30; -; 2.
DR   InterPro; IPR006108; 3HC_DH_C.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   Pfam; PF00725; 3HCDH; 1.
DR   SMART; SM00135; LY; 4.
DR   SUPFAM; SSF48179; SSF48179; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..475
FT                   /note="3-hydroxyacyl-CoA dehydrogenase-like protein LAM1"
FT                   /id="PRO_0000437648"
FT   BINDING         99..104
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q16836"
FT   BINDING         149
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q16836"
FT   BINDING         245
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q16836"
SQ   SEQUENCE   475 AA;  53486 MW;  5A4DDB68C9D08607 CRC64;
     MTPSAKRRTL NTHYFMPPHV RVVELMTSGN TAPEIMSLLV DRMKTVGLKP FVAKRESTGF
     IQNRVWASIK REMLHVVAEG IVDAQTADDI FVETIVRPGT RPFAAMDYVG LDTVANIERT
     YAQERHLDTT YTVDYLQREF IDVGKLGIKS NKGGFYPPST AADAVSTKPR IFVLDNGLSG
     QIDNLKQGKI LEYSFEGEYI RTVFKDQYLP DGIAVSQEEN VLFWTCMGSP GQKDGMIYAG
     KLDGNDIRPL IQQGIVHTPK QIVIDEANKK LYFTDREGLC IWRCDKDGSN LEQVVVTGDN
     NNECDRRDAT RWCVGITFSH TLGKIFWTQK GASKGWQGRI FSANMTIPPG ETAAHRKDKV
     CLLEGLAEPI DLDFHESTKT LYWTDRGEMP FGNTLNRLRF DDRGYALHTD STPHLKHEII
     ARKFHEAIGL KIDARNEHVY VADLGGSICR CKLDGSDKVR LVFQEDRAWT GVALA